Comparison of metal-bound and unbound structures of aminopeptidase B proteins from Escherichia coli and Yersinia pestis.
Escherichia coli
Yersinia pestis
PepB
X-ray crystallography
aminopeptidase
hexamer
metalloprotease
Journal
Protein science : a publication of the Protein Society
ISSN: 1469-896X
Titre abrégé: Protein Sci
Pays: United States
ID NLM: 9211750
Informations de publication
Date de publication:
07 2020
07 2020
Historique:
received:
09
02
2020
revised:
14
04
2020
accepted:
14
04
2020
pubmed:
20
4
2020
medline:
16
1
2021
entrez:
20
4
2020
Statut:
ppublish
Résumé
Protein degradation by aminopeptidases is involved in bacterial responses to stress. Escherichia coli produces two metal-dependent M17 family leucine aminopeptidases (LAPs), aminopeptidase A (PepA) and aminopeptidase B (PepB). Several structures have been solved for PepA as well as other bacterial M17 peptidases. Herein, we report the first structures of a PepB M17 peptidase. The E. coli PepB protein structure was determined at a resolution of 2.05 and 2.6 Å. One structure has both Zn
Identifiants
pubmed: 32306515
doi: 10.1002/pro.3876
pmc: PMC7314395
doi:
Substances chimiques
Escherichia coli Proteins
0
Manganese
42Z2K6ZL8P
Aminopeptidases
EC 3.4.11.-
Zinc
J41CSQ7QDS
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1618-1628Subventions
Organisme : NIAID NIH HHS
ID : U01 AI124316
Pays : United States
Organisme : NIAID NIH HHS
ID : U01AI124316
Pays : United States
Organisme : NIAID NIH HHS
ID : HHSN272201700060C
Pays : United States
Organisme : NIAID NIH HHS
ID : HHSN272201200026C
Pays : United States
Informations de copyright
© 2020 The Protein Society.
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